The Experts below are selected from a list of 30570 Experts worldwide ranked by ideXlab platform
Katsunori Teranishi - One of the best experts on this subject based on the ideXlab platform.
-
Bioluminescence and chemiluminescence abilities of trans 3 hydroxyhispidin on the luminous fungus mycena chlorophos
Luminescence, 2018Co-Authors: Katsunori TeranishiAbstract:The fungus Mycena chlorophos emits green light from its pileus gills but not from its stipes. The chemical mechanisms underlying its Bioluminescence are unclear. Trans-3-hydroxyhispidin has been known to be a luminescence substrate for the bioluminescent mycelia of Neonothopanus nambi and N. gardneri. In the present study, the Bioluminescence and chemiluminescence abilities of trans-3-hydroxyhispidin on pileus gills and originally non-bioluminescent stipes of M. chlorophos were demonstrated. Trans-3-hydroxyhispidin induced Bioluminescence of living gills and stipes. The Bioluminescence spectra of living gills and stipes measured after the addition of trans-3-hydroxyhispidin were consistent with the original Bioluminescence spectrum of gills. Frozen-thawed (dead) gills and stipes maintained trans-3-hydroxyhispidin luminescence activity, and the luminescence-active enzyme (luciferase) was partially purified in the water-insoluble state from both tissues using gel filtration followed by ultracentrifugation. The optimum temperature of the chemiluminescence reactions of trans-3-hydroxyhispidin in the presence of partially purified gill or stipe luciferase was 25°C. The chemiluminescence quantum yields of trans-3-hydroxyhispidin for gill luciferase and stipe luciferase in 20 mM phosphate buffer at 25°C were 0.017 and 0.00096, respectively and the chemiluminescence spectra were almost consistent with the Bioluminescence spectrum of living gills. These results indicate that trans-3-hydroxyhispidin can be a candidate as a substrate for M. chlorophos Bioluminescence.
-
trans 3 hydroxyhispidin is not an actual Bioluminescence substrate in pileus gills of the luminous fungus mycena chlorophos
Biochemical and Biophysical Research Communications, 2018Co-Authors: Katsunori TeranishiAbstract:Mycena chlorophos is a species of molecular oxygen-dependent bioluminescent fungus, and its pileus gills emit bright green light. The chemical mechanisms underlying this Bioluminescence phenomenon are not yet understood. An enzyme (luciferase) producing light from trans-3-hydroxyhispidin is present in M. chlorophos pileus gills. However, it is unclear whether trans-3-hydroxyhispidin is an actual Bioluminescence substrate (luciferin) in the natural Bioluminescence of M. chlorophos. In the present study, this question is resolved. It was clearly demonstrated that the trans-3-hydroxyhispidin analog trans-3-hydroxybisnoryangonin significantly inhibited the artificial luminescence induced by the addition of trans-3-hydroxyhispidin to living pileus gills but did not inhibit natural Bioluminescence in living pileus gills. This inhibition was due to the reaction of trans-3-hydroxybisnoryangonin with luciferase for trans-3-hydroxyhispidin. Even though trans-4-aminocinnamic acid is known to inhibit natural Bioluminescence in living pileus gills, in the present study, trans-4-aminocinnamic acid did not influence the artificial luminescence via trans-3-hydroxyhispidin in the presence of luciferase for trans-3-hydroxyhispidin. These inconsistencies between the natural Bioluminescence and the artificial luminescence of trans-3-hydroxyhispidin indicate that trans-3-hydroxyhispidin is not an actual luciferin in natural Bioluminescence. Trans-3,4-dihydroxycinnamic acid is generally known to be an intermediate in trans-3-hydroxyhispidin biosynthesis. The artificial luminescence induced by the addition of trans-3,4-dihydroxycinnamic acid to living pileus gills was not inhibited by trans-3-hydroxybisnoryangonin. Therefore, trans-3,4-dihydroxycinnamic acid does not contribute to the luminescence involving trans-3-hydroxyhispidin in living pileus gills.
-
inhibition of Bioluminescence in the living gills of the luminous fungus mycena chlorophos by trans 4 aminocinnamic acid
Biochemical and Biophysical Research Communications, 2017Co-Authors: Katsunori TeranishiAbstract:The living gills of the fungus Mycena chlorophos spontaneously emit green light. It was previously reported that trans-4-hydroxycinnamic acid and trans-3,4-dihydroxycinnnamic acid are essential for the bright light production in the living gills. However, the chemical mechanisms underlying their Bioluminescence are unknown. In the present study, trans-4-aminocinnamic acid was found to inhibit light production in the living gills. The concentrations of trans-4-aminocinnamic acid that inhibited the Bioluminescence intensity by 50% of initial values for immature and mature gills were 0.07 μM and 4 μM, respectively. Approximately 20% of the Bioluminescence intensity of the immature and mature gills was not inhibited by a further increase in the concentration of trans-4-aminocinnamic acid. Moreover, the Bioluminescence that was activated by trans-4-hydroxycinnamic acid or trans-3,4-dihydroxycinnamic acid (0.01 mM) was completely inhibited by trans-4-aminocinnamic acid. Therefore, trans-4-hydroxycinnamic acid and trans-3,4-dihydroxycinnamic acid functioned for the Bioluminescence that was inhibited by trans-4-aminocinnamic acid. trans-4-Aminocinnamic acid strongly bound to the Bioluminescence system(s) and withstood rinsing of the gills with 10 mM phosphate buffer (pH = 7), and high concentrations of trans-4-hydroxycinnamic acid (1 mM) and trans-3,4-dihydroxycinnamic acid (0.1 mM) functioned to displace trans-4-aminocinnamic acid from the Bioluminescence system(s) and reactivate Bioluminescence. Benzenamine, trans-cinnamic acid, trans-2-aminocinnamic acid, and trans-3-aminocinnamic acid did not inhibit Bioluminescence. Therefore, the structure-specific inhibition by trans-4-aminocinnamic acid suggested that the 4-hydroxy group in trans-4-hydroxycinnamic acid and trans-3,4-dihydroxycinnamic acid molecules plays a functional role in the Bioluminescence reaction.
-
second Bioluminescence activating component in the luminous fungus mycena chlorophos
Luminescence, 2017Co-Authors: Katsunori TeranishiAbstract:Mycena chlorophos is an oxygen-dependent bioluminescent fungus. The mechanisms underlying its light emission are unknown. A component that increased the Bioluminescence intensity of the immature living gills of M. chlorophos was isolated from mature M. chlorophos gills and chemically characterized. The Bioluminescence-activating component was found to be trans-3,4-dihydroxycinnamic acid and its Bioluminescence activation was highly structure-specific. 13 C- and 18 O-labelling studies using the immature living gills showed that trans-3,4-dihydroxycinnamic acid was synthesized from trans-4-hydroxycinnamic acid in the gills by hydroxylation with molecular oxygen as well as by the general metabolism, and trans-3,4-dihydroxycinnamic acid did not produce hispidin (detection-limit concentration: 10 pmol/1 g wet gill). Addition of 0.01 mM hispidin to the immature living gills generated no Bioluminescence activation. These results suggested that the prompt Bioluminescence activation resulting from addition of trans-3,4-dihydroxycinnamic acid could not be attributed to the generation of hispidin. Copyright © 2016 John Wiley & Sons, Ltd.
-
a combination of nadhp and hispidin is not essential for Bioluminescence in luminous fungal living gills of mycena chlorophos
Luminescence, 2017Co-Authors: Katsunori TeranishiAbstract:The chemical mechanisms underlying visible Bioluminescence in the fungus Mycena chlorophos are not clear. A combination of dihydronicotinamide adenine dinucleotide phosphate (NADPH) and hispidin, which has been reported to increase the intensity of in vitro luminescence in crude cold-water extracts prepared from the bioluminescent fruiting bodies of M. chlorophos, exhibited potential Bioluminescence activation in the early Bioluminescence stages, in which the Bioluminescence was ultra-weak, for living gills and luminescence activation for non-bioluminescent gills, which was collapsed by freezing and subsequent thawing, at all Bioluminescence stages. These abilities were not evident in considerably bioluminescent gills. These abilities were blocked by trans-4-hydroxycinnamic acid and trans-3,4-dihydroxycinnamic acid, which were identified as in vivo Bioluminescence-activating components. Original Bioluminescence and Bioluminescence produced from the addition of trans-4-hydroxycinnamic acid and trans-3,4-dihydroxycinnamic acid in living gills were almost completely inhibited by 10 mM NaN3, whereas the luminescence produced form the combination of NADPH and hispidin in thawed non-bioluminescent and living gills at the early weak Bioluminescence stages was not inhibited by 10 mM NaN3. Thus, the combination of NADPH and hispidin plays different roles in luminescence systems compared with essential Bioluminescence systems, and the combination of NADPH and hispidin was not essential for visible Bioluminescence in living gills.
Takashi Hirano - One of the best experts on this subject based on the ideXlab platform.
-
Toward Bioluminescence in the near-infrared region: Tuning the emission wavelength of firefly luciferin analogues by allyl substitution
Tetrahedron Letters, 2018Co-Authors: Nobuo Kitada, Tsuyoshi Saitoh, Yuma Ikeda, Satoshi Iwano, Rika Obata, Haruki Niwa, Takashi Hirano, Atsushi Miyawaki, Koji Suzuki, Shigeru NishiyamaAbstract:Abstract The synthesis and Bioluminescence of allyl-substituted luciferin derivatives as substrates for firefly luciferase are reported. The allylation of luciferins induced bathochromic shift (15–40 nm) of the Bioluminescence emission. Upon combination with other chemical modifications for Bioluminescence wavelength tuning, novel red emitting luciferin analogues were obtained with emission maxima at 685 and 690 nm.
-
quantum yield improvement of red light emitting firefly luciferin analogues for in vivo Bioluminescence imaging
Tetrahedron, 2017Co-Authors: Masahiro Kiyama, Satoshi Iwano, Rika Obata, Takashi Hirano, Atsushi Miyawaki, Satoshi Otsuka, Shojiro MakiAbstract:Abstract The dimethylamino group of AkaLumine ((4S)-2-[(1E,3E)-4-[4-(dimethylamino)phenyl]-1,3-butadien-1-yl]-4,5-dihydro-4-thiazolecarboxylic acid), a red-light-emitting firefly luciferin analogue, was replaced by cyclic amino groups (1-pyrrolidinyl, 1-piperidino, 1-azepanyl, and 4-morpholino) to give AkaLumine analogues exhibiting desirable Bioluminescence with emission maxima in the red region (656–667 nm). In particular, a Bioluminescence reaction of 1-pyrrolidinyl analogue with a recombinant Photinus pyralis luciferase showed a higher quantum yield than that with AkaLumine, giving an improved Bioluminescence intensity. The 1-pyrrolidinyl analogue also showed the strongest luminescence in whole-body luciferase-expressing mice among the analogues, indicating that a quantum yield improvement of a luciferin analogue is effective to increase Bioluminescence imaging intensity.
-
Bioluminescence of beetle luciferases with 6 amino d luciferin analogues reveals excited keto oxyluciferin as the emitter and phenolate luciferin binding site interactions modulate Bioluminescence colors
Biochemistry, 2014Co-Authors: Vadim R Viviani, Danilo T Amaral, Rogilene A. Prado, Deimison Rodrigues Neves, Takuto Matsuhashi, Takashi HiranoAbstract:Beetle luciferases produce different Bioluminescence colors from green to red using the same d-luciferin substrate. Despite many studies of the mechanisms and structural determinants of Bioluminescence colors with firefly luciferases, the identity of the emitters and the specific active site interactions responsible for Bioluminescence color modulation remain elusive. To address these questions, we analyzed the Bioluminescence spectra with 6′-amino-d-luciferin (aminoluciferin) and its 5,5-dimethyl analogue using a set of recombinant beetle luciferases that naturally elicit different colors and different pH sensitivities (pH-sensitive, Amydetes vivianii λmax = 538 nm, Macrolampis sp2 λmax = 564 nm; pH-insensitive, Phrixotrix hirtus λmax = 623 nm, Phrixotrix vivianii λmax = 546 nm, and Pyrearinus termitilluminans λmax = 534 nm), a luciferase-like enzyme (Tenebrionidae, Zophobas morio λmax = 613 nm), and mutants of C311 (S314). The green-yellow-emitting luciferases display red-shifted Bioluminescence spectra...
-
spectroscopic studies of the color modulation mechanism of firefly beetle Bioluminescence with amino analogs of luciferin and oxyluciferin
Photochemical and Photobiological Sciences, 2012Co-Authors: Takashi Hirano, Satoshi Iwano, Haruki Niwa, Takuto Matsuhashi, Shojiro Maki, Hiroyuki Nagai, Yosuke Hasumi, Kazuto Ito, Vadim R VivianiAbstract:Spectroscopic properties of amino-analogs of luciferin and oxyluciferin were investigated to confirm the color modulation mechanism of firefly (beetle) Bioluminescence. Fluorescence solvatochromic character of aminooxyluciferin analogs indicates that the Bioluminescence of aminoluciferin is useful for evaluating the polarity of a luciferase active site.
-
real light emitter in the Bioluminescence of the calcium activated photoproteins aequorin and obelin light emission from the singlet excited state of coelenteramide phenolate anion in a contact ion pair
Tetrahedron, 2006Co-Authors: Kotaro Mori, Haruki Niwa, Shojiro Maki, Hiroshi Ikeda, Takashi HiranoAbstract:Abstract Fluorescence of the phenolate anion ( 3 ( O ) − ) and the amide anion ( 5 ( N ) − ) of coelenteramide analogues in ion pairs with various counter cations was systematically investigated to elucidate the ionic structure of the light emitter in the Bioluminescence of the calcium-activated photoproteins aequorin and obelin. The fluorescent properties of 3 ( O ) − in an ion pair with a conjugate acid of an organic base (BASE–H + ) were varied depending on the structural variation of the ion pair and the solvent polarity. In particular, the fluorescence of 3 ( O ) − in the ion pair with the conjugate acid of n -butylamine (NBA–H + ) indicates that the singlet-excited state of 3 ( O ) − ( 1 3 ( O ) −∗ ) and NBA–H + make a contact ion pair in which the fluorescence emission maxima of 3 ( O ) − is sensitive to the solvent polarity and the fluorescence quantum yields of 3 ( O ) − increase in a less polar solvent. The results also confirm that 1 3 ( O ) −∗ is a twisted intramolecular charge transfer state. By contrast, the fluorescence of 5 ( N ) − in an ion pair depends little on the BASE–H + or the solvent polarity. Based on these results, we conclude that the light emitter in aequorin and obelin Bioluminescences is the singlet-excited state of coelenteramide phenolate anion 2 ( O ) − ( 1 2 ( O ) −∗ ) in a contact ion pair with an imidazolium side chain of a histidine residue, which is located at the less polar active sites of the photoproteins. We also propose a mechanism for the Bioluminescence reaction, including the chemiexcitation process to give 1 2 ( O ) −∗ .
Shojiro Maki - One of the best experts on this subject based on the ideXlab platform.
-
an allylated firefly luciferin analogue with luciferase specific response in living cells
Chemical Communications, 2018Co-Authors: Yuma Ikeda, Nobuo Kitada, Tsuyoshi Saitoh, Shigeru Nishiyama, Shojiro Maki, Daniel Citterio, Kazuki Niwa, Takahiro Nakajima, Moritoshi Sato, Koji SuzukiAbstract:An allylated firefly luciferin was successfully synthesized and its Bioluminescence properties were evaluated. When applied to cellular imaging in combination with Eluc, which is one of the commercially available luciferases, this analogue displayed a luciferase-specific Bioluminescence signal with prolonged emission (>100 min).
-
quantum yield improvement of red light emitting firefly luciferin analogues for in vivo Bioluminescence imaging
Tetrahedron, 2017Co-Authors: Masahiro Kiyama, Satoshi Iwano, Rika Obata, Takashi Hirano, Atsushi Miyawaki, Satoshi Otsuka, Shojiro MakiAbstract:Abstract The dimethylamino group of AkaLumine ((4S)-2-[(1E,3E)-4-[4-(dimethylamino)phenyl]-1,3-butadien-1-yl]-4,5-dihydro-4-thiazolecarboxylic acid), a red-light-emitting firefly luciferin analogue, was replaced by cyclic amino groups (1-pyrrolidinyl, 1-piperidino, 1-azepanyl, and 4-morpholino) to give AkaLumine analogues exhibiting desirable Bioluminescence with emission maxima in the red region (656–667 nm). In particular, a Bioluminescence reaction of 1-pyrrolidinyl analogue with a recombinant Photinus pyralis luciferase showed a higher quantum yield than that with AkaLumine, giving an improved Bioluminescence intensity. The 1-pyrrolidinyl analogue also showed the strongest luminescence in whole-body luciferase-expressing mice among the analogues, indicating that a quantum yield improvement of a luciferin analogue is effective to increase Bioluminescence imaging intensity.
-
a luciferin analogue generating near infrared Bioluminescence achieves highly sensitive deep tissue imaging
Nature Communications, 2016Co-Authors: Takahiro Kuchimaru, Satoshi Iwano, Haruki Niwa, Masahiro Kiyama, Shojiro Maki, Shun Mitsumata, Tetsuya Kadonosono, Shinae KizakakondohAbstract:In preclinical cancer research, Bioluminescence imaging with firefly luciferase and D-luciferin has become a standard to monitor biological processes both in vitro and in vivo. However, the emission maximum (λmax) of Bioluminescence produced by D-luciferin is 562 nm where light is not highly penetrable in biological tissues. This emphasizes a need for developing a red-shifted Bioluminescence imaging system to improve detection sensitivity of targets in deep tissue. Here we characterize the bioluminescent properties of the newly synthesized luciferin analogue, AkaLumine-HCl. The Bioluminescence produced by AkaLumine-HCl in reactions with native firefly luciferase is in the near-infrared wavelength ranges (λmax=677 nm), and yields significantly increased target-detection sensitivity from deep tissues with maximal signals attained at very low concentrations, as compared with D-luciferin and emerging synthetic luciferin CycLuc1. These characteristics offer a more sensitive and accurate method for non-invasive Bioluminescence imaging with native firefly luciferase in various animal models. D-luciferin is the standard bioluminescent substrate for in vitro and in vivo imaging. Here the authors introduce AkaLumine-HCl, a soluble luciferin analogue with a near-infrared emission maximum, which allows deep tissue imaging at lower concentrations than D-luciferin.
-
spectroscopic studies of the color modulation mechanism of firefly beetle Bioluminescence with amino analogs of luciferin and oxyluciferin
Photochemical and Photobiological Sciences, 2012Co-Authors: Takashi Hirano, Satoshi Iwano, Haruki Niwa, Takuto Matsuhashi, Shojiro Maki, Hiroyuki Nagai, Yosuke Hasumi, Kazuto Ito, Vadim R VivianiAbstract:Spectroscopic properties of amino-analogs of luciferin and oxyluciferin were investigated to confirm the color modulation mechanism of firefly (beetle) Bioluminescence. Fluorescence solvatochromic character of aminooxyluciferin analogs indicates that the Bioluminescence of aminoluciferin is useful for evaluating the polarity of a luciferase active site.
-
real light emitter in the Bioluminescence of the calcium activated photoproteins aequorin and obelin light emission from the singlet excited state of coelenteramide phenolate anion in a contact ion pair
Tetrahedron, 2006Co-Authors: Kotaro Mori, Haruki Niwa, Shojiro Maki, Hiroshi Ikeda, Takashi HiranoAbstract:Abstract Fluorescence of the phenolate anion ( 3 ( O ) − ) and the amide anion ( 5 ( N ) − ) of coelenteramide analogues in ion pairs with various counter cations was systematically investigated to elucidate the ionic structure of the light emitter in the Bioluminescence of the calcium-activated photoproteins aequorin and obelin. The fluorescent properties of 3 ( O ) − in an ion pair with a conjugate acid of an organic base (BASE–H + ) were varied depending on the structural variation of the ion pair and the solvent polarity. In particular, the fluorescence of 3 ( O ) − in the ion pair with the conjugate acid of n -butylamine (NBA–H + ) indicates that the singlet-excited state of 3 ( O ) − ( 1 3 ( O ) −∗ ) and NBA–H + make a contact ion pair in which the fluorescence emission maxima of 3 ( O ) − is sensitive to the solvent polarity and the fluorescence quantum yields of 3 ( O ) − increase in a less polar solvent. The results also confirm that 1 3 ( O ) −∗ is a twisted intramolecular charge transfer state. By contrast, the fluorescence of 5 ( N ) − in an ion pair depends little on the BASE–H + or the solvent polarity. Based on these results, we conclude that the light emitter in aequorin and obelin Bioluminescences is the singlet-excited state of coelenteramide phenolate anion 2 ( O ) − ( 1 2 ( O ) −∗ ) in a contact ion pair with an imidazolium side chain of a histidine residue, which is located at the less polar active sites of the photoproteins. We also propose a mechanism for the Bioluminescence reaction, including the chemiexcitation process to give 1 2 ( O ) −∗ .
Stefan W Hell - One of the best experts on this subject based on the ideXlab platform.
-
autonomous Bioluminescence imaging of single mammalian cells with the bacterial Bioluminescence system
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Carola Gregor, Jasmin K Pape, Klaus C Gwosch, Tanja Gilat, Steffen J Sahl, Stefan W HellAbstract:Bioluminescence-based imaging of living cells has become an important tool in biological and medical research. However, many Bioluminescence imaging applications are limited by the requirement of an externally provided luciferin substrate and the low Bioluminescence signal which restricts the sensitivity and spatiotemporal resolution. The bacterial Bioluminescence system is fully genetically encodable and hence produces autonomous Bioluminescence without an external luciferin, but its brightness in cell types other than bacteria has, so far, not been sufficient for imaging single cells. We coexpressed codon-optimized forms of the bacterial luxCDABE and frp genes from multiple plasmids in different mammalian cell lines. Our approach produces high luminescence levels that are comparable to firefly luciferase, thus enabling autonomous Bioluminescence microscopy of mammalian cells.
-
autonomous Bioluminescence imaging of single mammalian cells with the bacterial Bioluminescence system
bioRxiv, 2019Co-Authors: Carola Gregor, Jasmin K Pape, Klaus C Gwosch, Tanja Gilat, Steffen J Sahl, Stefan W HellAbstract:Abstract Bioluminescence based imaging of living cells has become an important tool in biological and medical research. However, many Bioluminescence imaging applications are limited by the requirement of an externally provided luciferin substrate and the low Bioluminescence signal which restricts the sensitivity and spatiotemporal resolution. The bacterial Bioluminescence system is fully genetically encodable and hence produces autonomous Bioluminescence without an external luciferin, but its brightness in cell types other than bacteria has so far not been sufficient for imaging single cells. We coexpressed codon-optimized forms of the bacterial luxCDABE and frp genes from multiple plasmids in different mammalian cell lines. Our approach produces high luminescence levels that are comparable to firefly luciferase, thus enabling autonomous Bioluminescence microscopy of mammalian cells. Significance statement Bioluminescence is generated by luciferases that oxidize a specific luciferin. The enzymes involved in the synthesis of the luciferin from widespread cellular metabolites have so far been identified for only two Bioluminescence systems, those of bacteria and fungi. In these cases, the complete reaction cascade is genetically encodable, meaning that heterologous expression of the corresponding genes can potentially produce autonomous Bioluminescence in cell types other than the bacterial or fungal host cells. However, the light levels achieved in mammalian cells so far are not sufficient for single-cell applications. Here we present, for the first time, autonomous Bioluminescence images of single mammalian cells by coexpression of the genes encoding the six enzymes from the bacterial Bioluminescence system.
Tianyu Jiang - One of the best experts on this subject based on the ideXlab platform.
-
bioluminescent properties of semi synthetic obelin and aequorin activated by coelenterazine analogues with modifications of c 2 c 6 and c 8 substituents
International Journal of Molecular Sciences, 2020Co-Authors: Elena V. Eremeeva, Natalia P Malikova, Tianyu Jiang, Eugene S VysotskiAbstract:Ca2+-regulated photoproteins responsible for Bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type Bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific Bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient Bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein Bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different Bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.
-
new bioluminescent coelenterazine derivatives with various c 6 substitutions
Organic and Biomolecular Chemistry, 2017Co-Authors: Tianyu Jiang, Xingye Yang, Yubin Zhou, Ilia V YampolskyAbstract:A series of new coelenterazine analogs with varying substituents at the C-6 position of the imidazopyrazinone core have been designed and synthesized for the extension of Bioluminescence substrates. Some of them display excellent Bioluminescence properties compared to DeepBlueC™ or native coelenterazine with both in vitro and in vivo biological evaluations, thus placing these derivatives among the most ideal substrates for Renilla Bioluminescence applications.
-
novel bioluminescent coelenterazine derivatives with imidazopyrazinone c 6 extended substitution for renilla luciferase
Organic and Biomolecular Chemistry, 2016Co-Authors: Tianyu Jiang, Mingliang Yuan, Xingye Yang, Xiaofeng Yang, Tianchao Zhang, Huateng ZhangAbstract:Two series of novel coelenterazine analogues (alkynes and triazoles) with imidazopyrazinone C-6 extended substitution have been designed and synthesized successfully for the extension of bioluminescent substrates. After extensive evaluation, some compounds display excellent Bioluminescence properties compared with DeepBlueC in cellulo, thus becoming potential molecules for Bioluminescence techniques.
-
lighting up Bioluminescence with coelenterazine strategies and applications
Photochemical and Photobiological Sciences, 2016Co-Authors: Tianyu JiangAbstract:Bioluminescence-based techniques, such as Bioluminescence imaging, BRET and dual-luciferase reporter assay systems, have been widely used to examine a myriad of biological processes. Coelenterazine (CTZ), a luciferin or light-producing compound found in bioluminescent organisms, has sparked great curiosity and interest in searching for analogues with improved photochemical properties. This review summarizes the current development of coelenterazine analogues, their Bioluminescence properties, and the rational design of caged coelenterazine towards biotargets, as well as their applications in bioassays. It should be emphasized that the design of caged luciferins can provide valuable insight into detailed molecular processes in organisms and will be a trend in the development of bioluminescent molecules.
-
Bioluminescent Probe for Detecting Mercury(II) in Living Mice
2016Co-Authors: Tianyu Jiang, Hui Chen, Weishan Wang, Keqian YangAbstract:A novel Bioluminescence probe for mercury(II) was obtained on the basis of the distinct deprotection reaction of dithioacetal to decanal, so as to display suitable sensitivity and selectivity toward mercury(II) over other ions with bacterial Bioluminescence signal. These experimental results indicated such a probe was a novel promising method for mercury(II) Bioluminescence imaging in environmental and life sciences ex vivo and in vivo